› 1xja

X-ray diffraction
2.4Å resolution

Apo form of the Y31V mutant dimerization domain fragment of Escherichia coli regulatory protein AraC

Released:
DOI: 10.2210/pdb1xja/pdb
PDB entry 1xja coloured by chain, front view.
PDB entry 1xja coloured by chain, side view.
PDB entry 1xja coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure and properties of a truely apo form of AraC dimerization domain.
Weldon JE, Rodgers ME, Larkin C, Schleif RF
Proteins 66 646-54 (2007)
PMID: 17173282

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141871 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arabinose operon regulatory protein Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 178 amino acids
Theoretical weight: 20.61 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A9E0 (Residues: 1-178; Coverage: 61%)
Gene names: JW0063, araC, b0064
Sequence domains: AraC-like ligand binding domain
Structure domains: Regulatory protein AraC

Ligands and Environments

1 bound ligand:
Ligand EDO 25 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: C2
Unit cell:
a: 260.632Å b: 40.621Å c: 102.589Å
α: 90° β: 105.45° γ: 90°
R-values:
R R work R free
0.239 0.211 0.256
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

AraC protein, regulation of the l-arabinose operon in Escherichia coli, and the light switch mechanism of AraC action.
Schleif R. (2010)
1 more

4 mentions without citation

Structure of Vibrio cholerae ToxT reveals a mechanism for fatty acid regulation of virulence genes.
Lowden et al. (2010)
3 more